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2000
Volume 8, Issue 3
  • ISSN: 1570-1646
  • E-ISSN: 1875-6247

Abstract

Human platelets are thought to express approximately 2000-3000 proteins, but post-translational modifications, alternatively spliced variants and a rich diversity of vertebrate domain architectures likely make this a conservative estimate. Even though rapidly advancing proteomic techniques have catalyzed the identification of roughly one third of the platelet proteome, a combination of abundance-based and activity-based proteomics is needed for elucidation of platelet functional characteristics including the definition of a “core proteome” and recognition of diverse enzyme activity profiles associated with various physiological states. In this review, we describe the latest mass spectrometry-based techniques capable of providing some of these physiological details required for more comprehensive evaluation of the human platelet repertoire.

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/content/journals/cp/10.2174/157016411797247512
2011-10-01
2025-12-11
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